Evolution of the folding landscape of effector caspases.
apoptosis
caspase
evolution
evolutionary biology
folding landscape
oligomerization
protease
protein evolution
protein folding
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
11 2021
11 2021
Historique:
received:
05
08
2021
revised:
22
09
2021
accepted:
23
09
2021
pubmed:
1
10
2021
medline:
16
12
2021
entrez:
30
9
2021
Statut:
ppublish
Résumé
Caspases are a family of cysteinyl proteases that control programmed cell death and maintain homeostasis in multicellular organisms. The caspase family is an excellent model to study protein evolution because all caspases are produced as zymogens (procaspases [PCPs]) that must be activated to gain full activity; the protein structures are conserved through hundreds of millions of years of evolution; and some allosteric features arose with the early ancestor, whereas others are more recent evolutionary events. The apoptotic caspases evolved from a common ancestor (CA) into two distinct subfamilies: monomers (initiator caspases) or dimers (effector caspases). Differences in activation mechanisms of the two subfamilies, and their oligomeric forms, play a central role in the regulation of apoptosis. Here, we examine changes in the folding landscape by characterizing human effector caspases and their CA. The results show that the effector caspases unfold by a minimum three-state equilibrium model at pH 7.5, where the native dimer is in equilibrium with a partially folded monomeric (PCP-7, CA) or dimeric (PCP-6) intermediate. In comparison, the unfolding pathway of PCP-3 contains both oligomeric forms of the intermediate. Overall, the data show that the folding landscape was first established with the CA and was retained for >650 million years. Partially folded monomeric or dimeric intermediates in the ancestral ensemble provide mechanisms for evolutionary changes that affect stability of extant caspases. The conserved folding landscape allows for the fine-tuning of enzyme stability in a species-dependent manner while retaining the overall caspase-hemoglobinase fold.
Identifiants
pubmed: 34592312
pii: S0021-9258(21)01052-8
doi: 10.1016/j.jbc.2021.101249
pmc: PMC8628267
pii:
doi:
Substances chimiques
Caspases, Effector
EC 3.4.22.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
101249Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM127654
Pays : United States
Informations de copyright
Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.
Références
Biochem J. 2019 Nov 29;476(22):3475-3492
pubmed: 31675069
Proteins. 2002 Mar 1;46(4):355-67
pubmed: 11835511
Mol Biol Evol. 2012 May;29(5):1353-66
pubmed: 22144639
Cold Spring Harb Perspect Biol. 2013 Apr 01;5(4):a008656
pubmed: 23545416
J Biol Chem. 2006 Mar 31;281(13):8667-74
pubmed: 16446367
PLoS One. 2007 May 16;2(5):e446
pubmed: 17505540
Biochemistry. 2013 Sep 10;52(36):6219-31
pubmed: 23941397
Biochem J. 2004 Dec 1;384(Pt 2):201-32
pubmed: 15450003
PLoS One. 2014 Oct 17;9(10):e110539
pubmed: 25330111
ACS Chem Biol. 2016 Jun 17;11(6):1603-12
pubmed: 27032039
Protein Sci. 2009 Dec;18(12):2500-17
pubmed: 19798740
Arch Biochem Biophys. 2013 Mar;531(1-2):44-64
pubmed: 23246784
J Biol Chem. 2020 Oct 23;295(43):14578-14591
pubmed: 32788218
Chem Rev. 2016 Jun 8;116(11):6666-706
pubmed: 26750439
J Mol Biol. 2002 Feb 15;316(2):327-40
pubmed: 11851342
Proc Natl Acad Sci U S A. 2013 Jul 23;110(30):E2821-8
pubmed: 23836639
Nucleic Acids Res. 2021 Jul 2;49(W1):W559-W566
pubmed: 34019657
Genes Dev. 2013 Sep 15;27(18):2039-48
pubmed: 24065769
J Biol Chem. 2001 Mar 9;276(10):7320-6
pubmed: 11058599
Methods Enzymol. 2014;544:215-49
pubmed: 24974292
Proc Natl Acad Sci U S A. 2010 Nov 23;107(47):20352-7
pubmed: 21048085
Proc Natl Acad Sci U S A. 2016 Nov 15;113(46):13045-13050
pubmed: 27799545
Nat Cell Biol. 2000 Jun;2(6):318-25
pubmed: 10854321
Adv Exp Med Biol. 2012;747:55-73
pubmed: 22949111
Protein Sci. 2018 Oct;27(10):1857-1870
pubmed: 30076665
J Biol Chem. 2018 Apr 13;293(15):5447-5461
pubmed: 29414778
Biopolymers. 2018 Aug;109(8):e23086
pubmed: 29152711
Nature. 2020 May;581(7809):480-485
pubmed: 32461643
Biochemistry. 2006 Nov 7;45(44):13249-63
pubmed: 17073446
Proc Natl Acad Sci U S A. 2019 Apr 2;116(14):6806-6811
pubmed: 30877249
Proc Natl Acad Sci U S A. 2016 Oct 11;113(41):E6080-E6088
pubmed: 27681633
Biochemistry. 2001 Nov 27;40(47):14236-42
pubmed: 11714277
Methods Enzymol. 2009;455:1-39
pubmed: 19289201
J Biol Chem. 2016 Aug 12;291(33):17450-66
pubmed: 27325699
Biochemistry. 2001 Nov 27;40(47):14224-35
pubmed: 11714276
Proc Natl Acad Sci U S A. 1996 Jan 23;93(2):654-8
pubmed: 8570610
Cell Chem Biol. 2019 Sep 19;26(9):1295-1305.e6
pubmed: 31353319
Biochemistry. 2013 May 21;52(20):3415-27
pubmed: 23614869
Proc Natl Acad Sci U S A. 2012 Nov 20;109(47):19244-9
pubmed: 23129648
Nat Rev Mol Cell Biol. 2007 Apr;8(4):319-30
pubmed: 17356578
Methods Enzymol. 2009;466:549-65
pubmed: 21609876
Protein Expr Purif. 2012 Aug;84(2):236-46
pubmed: 22683476
Protein Sci. 2016 Nov;25(11):2076-2088
pubmed: 27577093
J Phys Chem Lett. 2015 Jun 4;6(11):2022-6
pubmed: 26266496
Protein Sci. 2005 Jan;14(1):24-36
pubmed: 15576551
Proc Natl Acad Sci U S A. 2013 May 21;110(21):8477-82
pubmed: 23650375
Biochemistry. 2003 Oct 28;42(42):12298-310
pubmed: 14567691
J Mol Biol. 2019 Dec 6;431(24):4796-4816
pubmed: 31520601
Nat Rev Genet. 2013 Aug;14(8):559-71
pubmed: 23864121
J Biol Chem. 2019 Jan 4;294(1):71-88
pubmed: 30420425
Prog Biophys Mol Biol. 2008 Sep;98(1):61-84
pubmed: 18602415